ID B4RGT6_PHEZH Unreviewed; 229 AA.
AC B4RGT6;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=NAD(P)H dehydrogenase (quinone) {ECO:0000256|HAMAP-Rule:MF_01017};
DE EC=1.6.5.2 {ECO:0000256|HAMAP-Rule:MF_01017};
DE AltName: Full=NAD(P)H:quinone oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01017};
DE Short=NQO {ECO:0000256|HAMAP-Rule:MF_01017};
GN Name=wrbA {ECO:0000313|EMBL:ACG77302.1};
GN OrderedLocusNames=PHZ_c0888 {ECO:0000313|EMBL:ACG77302.1};
OS Phenylobacterium zucineum (strain HLK1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG77302.1, ECO:0000313|Proteomes:UP000001868};
RN [1] {ECO:0000313|EMBL:ACG77302.1, ECO:0000313|Proteomes:UP000001868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLK1 {ECO:0000313|EMBL:ACG77302.1,
RC ECO:0000313|Proteomes:UP000001868};
RX PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT "Complete genome of Phenylobacterium zucineum - a novel facultative
RT intracellular bacterium isolated from human erythroleukemia cell line
RT K562.";
RL BMC Genomics 9:386-386(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01017};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01017};
CC Note=Binds 1 FMN per monomer. {ECO:0000256|HAMAP-Rule:MF_01017};
CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000256|ARBA:ARBA00006961,
CC ECO:0000256|HAMAP-Rule:MF_01017}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01017}.
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DR EMBL; CP000747; ACG77302.1; -; Genomic_DNA.
DR AlphaFoldDB; B4RGT6; -.
DR STRING; 450851.PHZ_c0888; -.
DR KEGG; pzu:PHZ_c0888; -.
DR eggNOG; COG0655; Bacteria.
DR HOGENOM; CLU_051402_0_2_5; -.
DR OrthoDB; 9801479at2; -.
DR Proteomes; UP000001868; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR Gene3D; 3.40.50.360; -; 1.
DR HAMAP; MF_01017; NQOR; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR010089; Flavoprotein_WrbA-like.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR InterPro; IPR037513; NQO.
DR NCBIfam; TIGR01755; flav_wrbA; 1.
DR PANTHER; PTHR30546; FLAVODOXIN-RELATED PROTEIN WRBA-RELATED; 1.
DR PANTHER; PTHR30546:SF23; PROTEIN RFS1-RELATED; 1.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01017};
KW FMN {ECO:0000256|HAMAP-Rule:MF_01017};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01017};
KW NADP {ECO:0000256|HAMAP-Rule:MF_01017};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01017};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01017};
KW Reference proteome {ECO:0000313|Proteomes:UP000001868}.
FT DOMAIN 4..191
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT REGION 208..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..15
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 79..81
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 135
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
SQ SEQUENCE 229 AA; 24608 MW; 18F8B19B8C26BFAD CRC64;
MTKVLVLYHS TYGHIEAMAQ AVAEGAREIR GAQVDLKRVP ELVPEELARE SGYKLDQEAP
IATVAELEQY DAIVIGAGTR FGRIPSQMAS FLDQAGGLWA RGALNGKVGS AFTSTATQHG
GQETTLFSII TNLLHFGMCV VGLPYSFAGQ MTLDEITGGS PYGASTIAGG RGQRWPTRNE
LAAARFQGRL VAETAAKLGH GAQAMLRMDM SGPEQRSWED PREDDQPRA
//
